Full text data of PSMB6
PSMB6
(LMPY, Y)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteasome subunit beta type-6; 3.4.25.1 (Macropain delta chain; Multicatalytic endopeptidase complex delta chain; Proteasome delta chain; Proteasome subunit Y; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-6; 3.4.25.1 (Macropain delta chain; Multicatalytic endopeptidase complex delta chain; Proteasome delta chain; Proteasome subunit Y; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P28072
ID PSB6_HUMAN Reviewed; 239 AA.
AC P28072; Q96J55;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 4.
DT 22-JAN-2014, entry version 151.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1;
DE AltName: Full=Macropain delta chain;
DE AltName: Full=Multicatalytic endopeptidase complex delta chain;
DE AltName: Full=Proteasome delta chain;
DE AltName: Full=Proteasome subunit Y;
DE Flags: Precursor;
GN Name=PSMB6; Synonyms=LMPY, Y;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=8066462; DOI=10.1126/science.8066462;
RA Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T.,
RA Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
RT "cDNA cloning and interferon gamma down-regulation of proteasomal
RT subunits X and Y.";
RL Science 265:1231-1234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-9; 54-63 AND 210-230, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-239, AND PROTEIN SEQUENCE OF 35-75;
RP 80-110 AND 210-233.
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [5]
RP PROTEIN SEQUENCE OF 35-60.
RX PubMed=2306472; DOI=10.1016/0167-4838(90)90165-C;
RA Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA Slaughter C.A.;
RT "Relationships among the subunits of the high molecular weight
RT proteinase, macropain (proteasome).";
RL Biochim. Biophys. Acta 1037:178-185(1990).
RN [6]
RP PROTEIN SEQUENCE OF 157-178, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP SUBUNIT.
RX PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
RA Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M.,
RA Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
RT "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced
RT by interferon-gamma for acquirement of the functional diversity
RT responsible for antigen processing.";
RL FEBS Lett. 343:85-88(1994).
RN [8]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [9]
RP INDUCTION.
RX PubMed=15613457; DOI=10.1677/erc.1.00818;
RA Onda M., Emi M., Yoshida A., Miyamoto S., Akaishi J., Asaka S.,
RA Mizutani K., Shimizu K., Nagahama M., Ito K., Tanaka T., Tsunoda T.;
RT "Comprehensive gene expression profiling of anaplastic thyroid cancers
RT with cDNA microarray of 25 344 genes.";
RL Endocr. Relat. Cancer 11:843-854(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This unit is responsible of the peptidyl glutamyl-like
CC activity. May catalyze basal processing of intracellular antigens.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. This subunit can be displaced by
CC the equivalent immune-specific subunit PSMB9. Interacts with HIV-1
CC TAT protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level).
CC Up-regulated in anaplastic thyroid cancer cell lines.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D29012; BAA06098.1; -; mRNA.
DR EMBL; BC000835; AAH00835.1; -; mRNA.
DR EMBL; X61971; CAA43963.1; -; mRNA.
DR PIR; B54589; B54589.
DR PIR; S17522; S17522.
DR RefSeq; NP_002789.1; NM_002798.2.
DR UniGene; Hs.77060; -.
DR ProteinModelPortal; P28072; -.
DR SMR; P28072; 35-236.
DR IntAct; P28072; 14.
DR MINT; MINT-5004163; -.
DR STRING; 9606.ENSP00000270586; -.
DR ChEMBL; CHEMBL1944496; -.
DR MEROPS; T01.010; -.
DR PhosphoSite; P28072; -.
DR DMDM; 20532407; -.
DR OGP; P28072; -.
DR SWISS-2DPAGE; P28072; -.
DR PaxDb; P28072; -.
DR PeptideAtlas; P28072; -.
DR PRIDE; P28072; -.
DR DNASU; 5694; -.
DR Ensembl; ENST00000270586; ENSP00000270586; ENSG00000142507.
DR GeneID; 5694; -.
DR KEGG; hsa:5694; -.
DR UCSC; uc002fzb.4; human.
DR CTD; 5694; -.
DR GeneCards; GC17P004699; -.
DR HGNC; HGNC:9543; PSMB6.
DR HPA; HPA023312; -.
DR MIM; 600307; gene.
DR neXtProt; NX_P28072; -.
DR PharmGKB; PA33888; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091079; -.
DR HOVERGEN; HBG000123; -.
DR InParanoid; P28072; -.
DR KO; K02738; -.
DR OMA; TSIMAVQ; -.
DR OrthoDB; EOG79GT80; -.
DR PhylomeDB; P28072; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB6; human.
DR GeneWiki; PSMB6; -.
DR GenomeRNAi; 5694; -.
DR NextBio; 22118; -.
DR PRO; PR:P28072; -.
DR ArrayExpress; P28072; -.
DR Bgee; P28072; -.
DR CleanEx; HS_PSMB6; -.
DR Genevestigator; P28072; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 34 Removed in mature form.
FT /FTId=PRO_0000026613.
FT CHAIN 35 239 Proteasome subunit beta type-6.
FT /FTId=PRO_0000026614.
FT ACT_SITE 35 35 Nucleophile (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 107 107 P -> A (in dbSNP:rs2304974).
FT /FTId=VAR_020030.
FT CONFLICT 145 145 V -> G (in Ref. 1; BAA06098).
SQ SEQUENCE 239 AA; 25358 MW; 7DF4081DC735930C CRC64;
MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI
ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM
CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQSFA IGGSGSSYIY GYVDATYREG
MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
//
ID PSB6_HUMAN Reviewed; 239 AA.
AC P28072; Q96J55;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 4.
DT 22-JAN-2014, entry version 151.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1;
DE AltName: Full=Macropain delta chain;
DE AltName: Full=Multicatalytic endopeptidase complex delta chain;
DE AltName: Full=Proteasome delta chain;
DE AltName: Full=Proteasome subunit Y;
DE Flags: Precursor;
GN Name=PSMB6; Synonyms=LMPY, Y;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=8066462; DOI=10.1126/science.8066462;
RA Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T.,
RA Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
RT "cDNA cloning and interferon gamma down-regulation of proteasomal
RT subunits X and Y.";
RL Science 265:1231-1234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-9; 54-63 AND 210-230, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-239, AND PROTEIN SEQUENCE OF 35-75;
RP 80-110 AND 210-233.
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [5]
RP PROTEIN SEQUENCE OF 35-60.
RX PubMed=2306472; DOI=10.1016/0167-4838(90)90165-C;
RA Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA Slaughter C.A.;
RT "Relationships among the subunits of the high molecular weight
RT proteinase, macropain (proteasome).";
RL Biochim. Biophys. Acta 1037:178-185(1990).
RN [6]
RP PROTEIN SEQUENCE OF 157-178, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP SUBUNIT.
RX PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
RA Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M.,
RA Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
RT "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced
RT by interferon-gamma for acquirement of the functional diversity
RT responsible for antigen processing.";
RL FEBS Lett. 343:85-88(1994).
RN [8]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [9]
RP INDUCTION.
RX PubMed=15613457; DOI=10.1677/erc.1.00818;
RA Onda M., Emi M., Yoshida A., Miyamoto S., Akaishi J., Asaka S.,
RA Mizutani K., Shimizu K., Nagahama M., Ito K., Tanaka T., Tsunoda T.;
RT "Comprehensive gene expression profiling of anaplastic thyroid cancers
RT with cDNA microarray of 25 344 genes.";
RL Endocr. Relat. Cancer 11:843-854(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This unit is responsible of the peptidyl glutamyl-like
CC activity. May catalyze basal processing of intracellular antigens.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. This subunit can be displaced by
CC the equivalent immune-specific subunit PSMB9. Interacts with HIV-1
CC TAT protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level).
CC Up-regulated in anaplastic thyroid cancer cell lines.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D29012; BAA06098.1; -; mRNA.
DR EMBL; BC000835; AAH00835.1; -; mRNA.
DR EMBL; X61971; CAA43963.1; -; mRNA.
DR PIR; B54589; B54589.
DR PIR; S17522; S17522.
DR RefSeq; NP_002789.1; NM_002798.2.
DR UniGene; Hs.77060; -.
DR ProteinModelPortal; P28072; -.
DR SMR; P28072; 35-236.
DR IntAct; P28072; 14.
DR MINT; MINT-5004163; -.
DR STRING; 9606.ENSP00000270586; -.
DR ChEMBL; CHEMBL1944496; -.
DR MEROPS; T01.010; -.
DR PhosphoSite; P28072; -.
DR DMDM; 20532407; -.
DR OGP; P28072; -.
DR SWISS-2DPAGE; P28072; -.
DR PaxDb; P28072; -.
DR PeptideAtlas; P28072; -.
DR PRIDE; P28072; -.
DR DNASU; 5694; -.
DR Ensembl; ENST00000270586; ENSP00000270586; ENSG00000142507.
DR GeneID; 5694; -.
DR KEGG; hsa:5694; -.
DR UCSC; uc002fzb.4; human.
DR CTD; 5694; -.
DR GeneCards; GC17P004699; -.
DR HGNC; HGNC:9543; PSMB6.
DR HPA; HPA023312; -.
DR MIM; 600307; gene.
DR neXtProt; NX_P28072; -.
DR PharmGKB; PA33888; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091079; -.
DR HOVERGEN; HBG000123; -.
DR InParanoid; P28072; -.
DR KO; K02738; -.
DR OMA; TSIMAVQ; -.
DR OrthoDB; EOG79GT80; -.
DR PhylomeDB; P28072; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB6; human.
DR GeneWiki; PSMB6; -.
DR GenomeRNAi; 5694; -.
DR NextBio; 22118; -.
DR PRO; PR:P28072; -.
DR ArrayExpress; P28072; -.
DR Bgee; P28072; -.
DR CleanEx; HS_PSMB6; -.
DR Genevestigator; P28072; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 34 Removed in mature form.
FT /FTId=PRO_0000026613.
FT CHAIN 35 239 Proteasome subunit beta type-6.
FT /FTId=PRO_0000026614.
FT ACT_SITE 35 35 Nucleophile (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 107 107 P -> A (in dbSNP:rs2304974).
FT /FTId=VAR_020030.
FT CONFLICT 145 145 V -> G (in Ref. 1; BAA06098).
SQ SEQUENCE 239 AA; 25358 MW; 7DF4081DC735930C CRC64;
MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI
ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM
CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQSFA IGGSGSSYIY GYVDATYREG
MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
//
MIM
600307
*RECORD*
*FIELD* NO
600307
*FIELD* TI
*600307 PROTEASOME SUBUNIT, BETA-TYPE, 6; PSMB6
;;PROTEASOME SUBUNIT DELTA;;
PROTEASOME SUBUNIT Y;;
read morePSY LARGE MULTIFUNCTIONAL PROTEASE Y; LMPY;;
PROTEASOME SUBUNIT BETA-1
*FIELD* TX
CLONING
DeMartino et al. (1991) cloned a partial cDNA encoding the PSMB6
subunit, termed 'subunit delta.' Akiyama et al. (1994) cloned the
full-length cDNA, which encoded a 239-amino acid polypeptide. The amino
acid sequence has significant homology to other proteasome beta
subunits. See PSMB5 (600306).
GENE FUNCTION
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The beta subunits are believed to form the inner
rings of the proteasome and to mediate proteolysis.
MAPPING
Belich et al. (1994) mapped the PSMB6 gene to 17p13 by fluorescence in
situ hybridization.
*FIELD* RF
1. Akiyama, K.; Yokota, K.; Kagawa, S.; Shimbara, N.; Tamura, T.;
Akioka, H.; Nothwang, H. G.; Noda, C.; Tanaka, K.; Ichihara, A.:
cDNA cloning and interferon gamma down-regulation of proteasomal subunits
X and Y. Science 265: 1231-1234, 1994.
2. Belich, M. P.; Glynne, R. J.; Senger, G.; Sheer, D.; Trowsdale,
J.: Proteasome components with reciprocal expression to that of the
MHC-encoded LMP proteins. Curr. Biol. 4: 769-776, 1994.
3. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
4. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
*FIELD* CD
Victor A. McKusick: 1/11/1995
*FIELD* ED
alopez: 05/12/2009
mgross: 6/25/2007
kayiaros: 7/13/1999
alopez: 8/2/1998
dkim: 7/23/1998
alopez: 7/16/1998
mark: 12/12/1997
jamie: 1/29/1997
mark: 6/13/1995
carol: 1/11/1995
*RECORD*
*FIELD* NO
600307
*FIELD* TI
*600307 PROTEASOME SUBUNIT, BETA-TYPE, 6; PSMB6
;;PROTEASOME SUBUNIT DELTA;;
PROTEASOME SUBUNIT Y;;
read morePSY LARGE MULTIFUNCTIONAL PROTEASE Y; LMPY;;
PROTEASOME SUBUNIT BETA-1
*FIELD* TX
CLONING
DeMartino et al. (1991) cloned a partial cDNA encoding the PSMB6
subunit, termed 'subunit delta.' Akiyama et al. (1994) cloned the
full-length cDNA, which encoded a 239-amino acid polypeptide. The amino
acid sequence has significant homology to other proteasome beta
subunits. See PSMB5 (600306).
GENE FUNCTION
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The beta subunits are believed to form the inner
rings of the proteasome and to mediate proteolysis.
MAPPING
Belich et al. (1994) mapped the PSMB6 gene to 17p13 by fluorescence in
situ hybridization.
*FIELD* RF
1. Akiyama, K.; Yokota, K.; Kagawa, S.; Shimbara, N.; Tamura, T.;
Akioka, H.; Nothwang, H. G.; Noda, C.; Tanaka, K.; Ichihara, A.:
cDNA cloning and interferon gamma down-regulation of proteasomal subunits
X and Y. Science 265: 1231-1234, 1994.
2. Belich, M. P.; Glynne, R. J.; Senger, G.; Sheer, D.; Trowsdale,
J.: Proteasome components with reciprocal expression to that of the
MHC-encoded LMP proteins. Curr. Biol. 4: 769-776, 1994.
3. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
4. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
*FIELD* CD
Victor A. McKusick: 1/11/1995
*FIELD* ED
alopez: 05/12/2009
mgross: 6/25/2007
kayiaros: 7/13/1999
alopez: 8/2/1998
dkim: 7/23/1998
alopez: 7/16/1998
mark: 12/12/1997
jamie: 1/29/1997
mark: 6/13/1995
carol: 1/11/1995